Synthesis and Characterization of the Benzoylformato Ferrous Complexes with the Hindered Tris(pyrazolyl)borate Ligand as a Structural Model for Mononuclear Non-Heme Iron Enzymes†

1997 ◽  
Vol 36 (20) ◽  
pp. 4539-4547 ◽  
Author(s):  
Shiro Hikichi ◽  
Tamako Ogihara ◽  
Kiyoshi Fujisawa ◽  
Nobumasa Kitajima ◽  
Munetaka Akita ◽  
...  
Keyword(s):  
Structural Model ◽  
Heme Iron ◽  
Synthesis And Characterization ◽  
Non Heme Iron ◽  
Iron Enzymes

Synthesis and Characterization of Novel Alkylperoxo Mononuclear Iron(III) Complexes with a Tripodal Pyridylamine Ligand:  A Model for Peroxo Intermediates in Reactions Catalyzed by Non-Heme Iron Enzymes

1999 ◽  
Vol 38 (16) ◽  
pp. 3592-3593 ◽  
Author(s):  
Akira Wada ◽  
Seiji Ogo ◽  
Yoshihito Watanabe ◽  
Masahiro Mukai ◽  
Teizo Kitagawa ◽  
...  
Keyword(s):  
Heme Iron ◽  
Synthesis And Characterization ◽  
Mononuclear Iron ◽  
Non Heme Iron ◽  
Iron Enzymes

Synthesis and characterization of two binuclear iron(III) complexes of aminoethanol derivatives of aminophenol as models for non-heme iron enzymes active sites

Polyhedron ◽  
2011 ◽  
Vol 30 (6) ◽  
pp. 1143-1148 ◽  
Author(s):  
Elham Safaei ◽  
Iraj Saberikia ◽  
Andrzej Wojtczak ◽  
Zvonko Jagličić ◽  
Anna Kozakiewicz
Keyword(s):  
Active Sites ◽  
Heme Iron ◽  
Synthesis And Characterization ◽  
Non Heme Iron ◽  
Iron Enzymes ◽  
Derivatives Of ◽  
Binuclear Iron

Synthesis and characterization of a family of binuclear non-heme iron monooxygenase model compounds: Evidence for a “phenolate/amide carbonyl (PAC) shift” upon oxidation

2009 ◽  
Vol 362 (7) ◽  
pp. 2136-2150 ◽  
Author(s):  
Patrick J. Cappillino ◽  
Paul C. Tarves ◽  
Gerard T. Rowe ◽  
Andrew J. Lewis ◽  
Mark Harvey ◽  
...  
Keyword(s):  
Heme Iron ◽  
Synthesis And Characterization ◽  
Model Compounds ◽  
Non Heme Iron ◽  
Amide Carbonyl

Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD

2019 ◽  
Author(s):  
Christopher John ◽  
Greg M. Swain ◽  
Robert P. Hausinger ◽  
Denis A. Proshlyakov
Keyword(s):  
Active Site ◽  
Structural Model ◽  
Heme Iron ◽  
Chemical Transformations ◽  
Experimental Conditions ◽  
Strongly Coupled ◽  
Non Heme Iron ◽  
Reversible Redox ◽  
Wide Range ◽  
Complex Structural

2-Oxoglutarate (2OG)-dependent dioxygenases catalyze C-H activation while performing a wide range of chemical transformations. In contrast to their heme analogues, non-heme iron centers afford greater structural flexibility with important implications for their diverse catalytic mechanisms. We characterize an <i>in situ</i> structural model of the putative transient ferric intermediate of 2OG:taurine dioxygenase (TauD) by using a combination of spectroelectrochemical and semi-empirical computational methods, demonstrating that the Fe (III/II) transition involves a substantial, fully reversible, redox-linked conformational change at the active site. This rearrangement alters the apparent redox potential of the active site between -127 mV for reduction of the ferric state and 171 mV for oxidation of the ferrous state of the 2OG-Fe-TauD complex. Structural perturbations exhibit limited sensitivity to mediator concentrations and potential pulse duration. Similar changes were observed in the Fe-TauD and taurine-2OG-Fe-TauD complexes, thus attributing the reorganization to the protein moiety rather than the cosubstrates. Redox difference infrared spectra indicate a reorganization of the protein backbone in addition to the involvement of carboxylate and histidine ligands. Quantitative modeling of the transient redox response using two alternative reaction schemes across a variety of experimental conditions strongly supports the proposal for intrinsic protein reorganization as the origin of the experimental observations.

Theoretical studies of oxygen activation by non-heme iron enzymes

2003 ◽  
Vol 96 (1) ◽  
pp. 62
Author(s):  
Arianna Bassan ◽  
Margareta R.A. Blomberg ◽  
Per E.M. Siegbahn
Keyword(s):  
Oxygen Activation ◽  
Heme Iron ◽  
Theoretical Studies ◽  
Non Heme Iron ◽  
Iron Enzymes

Peroxo-Type Intermediates in Class I Ribonucleotide Reductase and Related Binuclear Non-Heme Iron Enzymes

2009 ◽  
Vol 131 (34) ◽  
pp. 12155-12171 ◽  
Author(s):  
Kasper P. Jensen ◽  
Caleb B. Bell, ◽  
Michael D. Clay ◽  
Edward I. Solomon
Keyword(s):  
Ribonucleotide Reductase ◽  
Heme Iron ◽  
Class I ◽  
Non Heme Iron ◽  
Iron Enzymes

Iron Complexes of Cyclam and Cyclam-Like Ligands as Models for Non-Heme Iron Enzymes

1993 ◽  
pp. 460-460
Author(s):  
Raymond Ho ◽  
Joan Selverstone Valentine
Keyword(s):  
Iron Complexes ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Iron Enzymes

ChemInform Abstract: Structural “Snapshots” along Reaction Pathways of Non-Heme Iron Enzymes

ChemInform ◽  
2008 ◽  
Vol 39 (7) ◽  
Author(s):  
Joseph P. Emerson ◽  
Erik R. Farquhar ◽  
Lawrence Jr. Que
Keyword(s):  
Heme Iron ◽  
Reaction Pathways ◽  
Non Heme Iron ◽  
Iron Enzymes
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